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Volumn 10, Issue 12, 2009, Pages 5498-5512

Contributions of the C-terminal helix to the structural stability of a hyperthermophilic Fe-superoxide dismutase (TcSOD)

Author keywords

Fe superoxide dismutase; Hyperthermophilic enzyme; Ion pairing network; Protein unfolding; Thermostability

Indexed keywords

GUANIDINE; IRON SUPEROXIDE DISMUTASE;

EID: 74249101357     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10125498     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille, C.; Zeikus, G.J. Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65, 1-43.
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 4
    • 34547747311 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications
    • Unsworth, L.D.; van der Oost, J.; Koutsopoulos, S. Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications. FEBS J. 2007, 274, 4044-4056.
    • (2007) FEBS J , vol.274 , pp. 4044-4056
    • Unsworth, L.D.1    van der Oost, J.2    Koutsopoulos, S.3
  • 5
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • Kumar, S.; Nussinov, R. How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 2001, 58, 1216-1233.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 6
  • 7
    • 0033548190 scopus 로고    scopus 로고
    • Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: Analysis of structure and thermostability
    • Ursby, T.; Adinolfi, B.S.; Al-Karadaghi, S.; de Vendittis, E.; Bocchini, V. Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: Analysis of structure and thermostability. J. Mol. Biol. 1999, 286, 189-205.
    • (1999) J. Mol. Biol , vol.286 , pp. 189-205
    • Ursby, T.1    Adinolfi, B.S.2    Al-Karadaghi, S.3    de Vendittis, E.4    Bocchini, V.5
  • 8
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
    • Thoma, R.; Hennig, M.; Sterner, R.; Kirschner, K. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure 2000, 8, 265-276.
    • (2000) Structure , vol.8 , pp. 265-276
    • Thoma, R.1    Hennig, M.2    Sterner, R.3    Kirschner, K.4
  • 9
    • 3543039400 scopus 로고    scopus 로고
    • How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii
    • Tanaka, Y.; Tsumoto, K.; Yasutake, Y.; Umetsu, M.; Yao, M.; Fukada, H.; Tanaka, I.; Kumagai, I. How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii. J. Biol. Chem. 2004, 279, 32957-32967.
    • (2004) J. Biol. Chem , vol.279 , pp. 32957-32967
    • Tanaka, Y.1    Tsumoto, K.2    Yasutake, Y.3    Umetsu, M.4    Yao, M.5    Fukada, H.6    Tanaka, I.7    Kumagai, I.8
  • 10
    • 43049149352 scopus 로고    scopus 로고
    • Multistate folding of a hyperthermostable Fe-superoxide dismutase (TcSOD) in guanidinium hydrochloride: The importance of the quaternary structure
    • Wang, S.; Liu, W.-F.; He, Y.-Z.; Zhang, A.; Huang, L.; Dong, Z.-Y.; Yan, Y.-B. Multistate folding of a hyperthermostable Fe-superoxide dismutase (TcSOD) in guanidinium hydrochloride: The importance of the quaternary structure. Biochim. Biophys. Acta: Prot. Proteom. 2008, 1784, 445-454.
    • (2008) Biochim. Biophys. Acta: Prot. Proteom , vol.1784 , pp. 445-454
    • Wang, S.1    Liu, W.-F.2    He, Y.-Z.3    Zhang, A.4    Huang, L.5    Dong, Z.-Y.6    Yan, Y.-B.7
  • 12
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 1995, 64, 97-112.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 13
    • 1842583981 scopus 로고    scopus 로고
    • Superoxide dismutases: Active sites that save, but a protein that kills
    • Miller, A.-F. Superoxide dismutases: Active sites that save, but a protein that kills. Curr. Opin. Chem. Biol. 2004, 8, 162-168.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 162-168
    • Miller, A.-F.1
  • 14
    • 0030914069 scopus 로고    scopus 로고
    • Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium
    • Lim, J.-H.; Yu, Y.G.; Choi, I.-G.; Ryu, J.-R.; Ahn, B.-Y.; Kim, S.-H.; Han, Y.-S. Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium. FEBS Lett. 1997, 406, 142-146.
    • (1997) FEBS Lett , vol.406 , pp. 142-146
    • Lim, J.-H.1    Yu, Y.G.2    Choi, I.-G.3    Ryu, J.-R.4    Ahn, B.-Y.5    Kim, S.-H.6    Han, Y.-S.7
  • 15
    • 0033555252 scopus 로고    scopus 로고
    • Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution
    • Knapp, S.; Kardinahl, S.; Hellgren, N.; Tibbelin, G.; Schäfer, G.; Ladenstein, R. Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution. J. Mol. Biol. 1999, 285, 689-702.
    • (1999) J. Mol. Biol , vol.285 , pp. 689-702
    • Knapp, S.1    Kardinahl, S.2    Hellgren, N.3    Tibbelin, G.4    Schäfer, G.5    Ladenstein, R.6
  • 16
    • 0034125824 scopus 로고    scopus 로고
    • Recombinant superoxide dismutase from a hyperthermophilic archaeon, Pyrobaculum aerophilium
    • Whittaker, M.M.; Whittaker, J.W. Recombinant superoxide dismutase from a hyperthermophilic archaeon, Pyrobaculum aerophilium. J. Biol. Inorg. Chem. 2000, 5, 402-408.
    • (2000) J. Biol. Inorg. Chem , vol.5 , pp. 402-408
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 18
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of a Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim, J.-H.; Yu, Y.G.; Han, Y.S.; Cho, S.-J.; Ahn, B.-Y.; Kim, S.-H.; Cho, Y. The crystal structure of a Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability. J. Mol. Biol. 1997, 270, 259-274.
    • (1997) J. Mol. Biol , vol.270 , pp. 259-274
    • Lim, J.-H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.-J.4    Ahn, B.-Y.5    Kim, S.-H.6    Cho, Y.7
  • 19
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A.; Serrano, L.; Avron, B.; Bycroft, M.; Fersht, A.R. Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 1990, 216, 1031-1044.
    • (1990) J. Mol. Biol , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 20
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little to stability of barnase
    • Bycroft, M.; Fersht, A.R. Surface electrostatic interactions contribute little to stability of barnase. J. Mol. Biol. 1991, 220, 779-788.
    • (1991) J. Mol. Biol , vol.220 , pp. 779-788
    • Bycroft, M.1    Fersht, A.R.2
  • 21
    • 0026584344 scopus 로고
    • Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
    • Shirley, B.A.; Stanssens, P.; Hahn, U.; Pace, C.N. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry 1992, 31, 725-732.
    • (1992) Biochemistry , vol.31 , pp. 725-732
    • Shirley, B.A.1    Stanssens, P.2    Hahn, U.3    Pace, C.N.4
  • 23
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G.; Woell, S.; Argos, P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 1997, 269, 631-643.
    • (1997) J. Mol. Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 24
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A "traffic rule" for hot roads
    • Karshikoff, A.; Ladenstein, R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: A "traffic rule" for hot roads. Trends Biochem. Sci. 2001, 26, 550-556.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 25
    • 0348047619 scopus 로고    scopus 로고
    • Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge
    • Leemhuis, H.; Rozeboom, H.J.; Dijkstra, B.W.; Dijkhuizen, L. Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge. Proteins 2004, 54, 128-134.
    • (2004) Proteins , vol.54 , pp. 128-134
    • Leemhuis, H.1    Rozeboom, H.J.2    Dijkstra, B.W.3    Dijkhuizen, L.4
  • 26
    • 24744447220 scopus 로고    scopus 로고
    • Identifying and engineering ion pairs in adenylate kinases. Insights from molecular dynamics simulations of thermophilic and mesophilic homologues
    • Bae, E.; Phillips, G.N., Jr. Identifying and engineering ion pairs in adenylate kinases. Insights from molecular dynamics simulations of thermophilic and mesophilic homologues. J. Biol. Chem. 2005, 280, 30943-30948.
    • (2005) J. Biol. Chem , vol.280 , pp. 30943-30948
    • Bae, E.1    Phillips Jr., G.N.2
  • 27
    • 32044454841 scopus 로고    scopus 로고
    • Effective factors in thermostability of thermophilic proteins
    • Sadeghi, M.; Naderi-Manesh, H.; Zarrabi, M.; Ranjbar, B. Effective factors in thermostability of thermophilic proteins. Biophys. Chem. 2006, 119, 256-270.
    • (2006) Biophys. Chem , vol.119 , pp. 256-270
    • Sadeghi, M.1    Naderi-Manesh, H.2    Zarrabi, M.3    Ranjbar, B.4
  • 28
    • 0035914001 scopus 로고    scopus 로고
    • Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: Understanding the molecular basis of protein thermostability
    • Lim, J.H.; Hwang, K.Y.; Choi, J.; Lee, D.Y.; Ahn, B.Y.; Cho, Y.; Kim, K.S.; Han, Y.S. Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: Understanding the molecular basis of protein thermostability. Biochem. Biophys. Res. Commun. 2001, 288, 263-268.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 263-268
    • Lim, J.H.1    Hwang, K.Y.2    Choi, J.3    Lee, D.Y.4    Ahn, B.Y.5    Cho, Y.6    Kim, K.S.7    Han, Y.S.8
  • 29
    • 0346788888 scopus 로고    scopus 로고
    • Iron superoxide dismutases: Structure and function of an archaic enzyme
    • Schafer, G.; Kardinahl, S. Iron superoxide dismutases: Structure and function of an archaic enzyme. Biochem. Soc. Trans. 2003, 31, 1330-1334.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1330-1334
    • Schafer, G.1    Kardinahl, S.2
  • 30
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret, V.; Clantin, B.; Tricot, C.; Legrain, C.; Roovers, M.; Stalon, V.; Glansdorff, N.; van Beeumen, J. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc. Natl. Acad. Sci. USA 1998, 95, 2801-2806.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    van Beeumen, J.8
  • 31
    • 0033769510 scopus 로고    scopus 로고
    • A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability
    • Shima, S.; Thauer, R.K.; Ermler, U.; Durchschlag, H.; Tziatzios, C.; Schubert, D. A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability. Eur. J. Biochem. 2000, 267, 6619-6623.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6619-6623
    • Shima, S.1    Thauer, R.K.2    Ermler, U.3    Durchschlag, H.4    Tziatzios, C.5    Schubert, D.6
  • 33
    • 0034851610 scopus 로고    scopus 로고
    • Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus
    • Ogasahara, K.; Khechinashvili, N.N.; Nakamura, M.; Yoshimoto, T.; Yutani, K. Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus. Eur. J. Biochem. 2001, 268, 3233-3242.
    • (2001) Eur. J. Biochem , vol.268 , pp. 3233-3242
    • Ogasahara, K.1    Khechinashvili, N.N.2    Nakamura, M.3    Yoshimoto, T.4    Yutani, K.5
  • 34
    • 33845227579 scopus 로고    scopus 로고
    • Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability
    • Feng, S.; Zhao, T.-J.; Zhou, H.-M.; Yan, Y.-B. Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability. Int. J. Biochem. Cell Biol. 2007, 39, 392-401.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 392-401
    • Feng, S.1    Zhao, T.-J.2    Zhou, H.-M.3    Yan, Y.-B.4
  • 35
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund, S.; Marklund, G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 1974, 47, 469-474.
    • (1974) Eur. J. Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 36
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 73, 248-254.
    • (1976) Anal. Biochem , vol.73 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0029981024 scopus 로고    scopus 로고
    • Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes
    • Tams, J.W.; Welinder, K.G. Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes. Biochemistry 1996, 35, 7573-7579.
    • (1996) Biochemistry , vol.35 , pp. 7573-7579
    • Tams, J.W.1    Welinder, K.G.2


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